2C7I
Structure of protein Ta0514, putative lipoate protein ligase from T. acidophilum.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.230, 118.356, 105.592 |
| Unit cell angles | 90.00, 93.75, 90.00 |
Refinement procedure
| Resolution | 19.870 - 2.100 |
| R-factor | 0.21 |
| Rwork | 0.208 |
| R-free | 0.25200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | SEE REMARK |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.254 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.870 | 2.170 |
| High resolution limit [Å] | 2.100 | 2.080 |
| Rmerge | 0.070 | 0.230 |
| Number of reflections | 68335 | |
| <I/σ(I)> | 22 | 6 |
| Completeness [%] | 95.3 | 72.3 |
| Redundancy | 10 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.7 | pH 6.70 |
